ID A7EQ37_SCLS1 Unreviewed; 757 AA.
AC A7EQ37;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Long-chain-alcohol oxidase {ECO:0000256|ARBA:ARBA00013125, ECO:0000256|PIRNR:PIRNR028937};
DE EC=1.1.3.20 {ECO:0000256|ARBA:ARBA00013125, ECO:0000256|PIRNR:PIRNR028937};
GN ORFNames=SS1G_07437 {ECO:0000313|EMBL:EDO04953.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDO04953.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- FUNCTION: Long-chain fatty alcohol oxidase involved in the omega-
CC oxidation pathway of lipid degradation.
CC {ECO:0000256|ARBA:ARBA00003842}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain primary fatty alcohol + O2 = a long-chain fatty
CC aldehyde + H2O2; Xref=Rhea:RHEA:22756, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17176, ChEBI:CHEBI:77396; EC=1.1.3.20;
CC Evidence={ECO:0000256|ARBA:ARBA00000920,
CC ECO:0000256|PIRNR:PIRNR028937};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|PIRNR:PIRNR028937}.
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DR EMBL; CH476629; EDO04953.1; -; Genomic_DNA.
DR RefSeq; XP_001591990.1; XM_001591940.1.
DR AlphaFoldDB; A7EQ37; -.
DR EnsemblFungi; EDO04953; EDO04953; SS1G_07437.
DR GeneID; 5487685; -.
DR KEGG; ssl:SS1G_07437; -.
DR VEuPathDB; FungiDB:sscle_06g049240; -.
DR eggNOG; ENOG502QSD8; Eukaryota.
DR HOGENOM; CLU_008878_3_1_1; -.
DR InParanoid; A7EQ37; -.
DR OMA; GCPTNAK; -.
DR OrthoDB; 601859at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046577; F:long-chain-alcohol oxidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR012400; Long_Oxdase.
DR PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PIRSF; PIRSF028937; Lg_Ch_AO; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR028937};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 273..499
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 590..730
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 637..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 679
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
SQ SEQUENCE 757 AA; 82767 MW; 7FF3741B0F3E5ACB CRC64;
MTSNTIDIIA PIVTPLPDPP EGQYFTDLQW STLMAIMDTV IPSIHKASIT NDPSSQLSVP
DEQYNDAVTY VRTTISSPPS DEALEAYLNE KPSDIPAFQD ILLRTLTTYA REDARKALSF
ILTTLNTRLG SLMLTGYASP LQSHPVNIRQ SILTNWRNSY FFPLRAIAKT MSLLGKHIWL
KTSPNFDKVT GFAKIPDHYK PGPHYEYEFL QFTASDEPQI IETDVVIVGS GCGGAVCAKN
LAEDGHKVLV VEKSYYFSPS HLPMSEATSG IHLFENGGVI MNDDSSMSIT AGSSWGGGGT
VNWSASLQTQ GFVRKEWAED RGLKFFGSTD FQECLDRVCE RMGVSAEHIR HSHGNQVLLE
GSRKLGFNAK SVPQNTGGHE HYCGHCSNGC GSSQKQGPTV SWLPDAAKAG AEFIEGFKVD
HVIFDEEDEK KAVGVKGVWT SRNSRGGVDG PLSDKIVREV IVKAKKVIIS TGTLWTPVIL
KNSGLTNSQI GRNLYLHPVS MVGAVFPEDV RPWEGGILTS VCTSFENLDS HGHGAKLEAT
CMMPSLCIST LNYPTGFESK FKSLLYRHMN VFISIARDRD TGIVYPDAKT GLPRISYTPS
EFDRGHIRQG VLALTKICYV SGAKEIHVTA SGINPYTRSP SSLSTDSNDP SSDPAFQTWL
TTLSNTSTKP PLSQFASAHQ MGTSRMSTRP ENGVVDPKGK VWDTENLYVS DASVFPSASG
VNPMITIMAI SDWISRGISQ ELKGNGGEEK VEERARL
//